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Significance We developed L-2-tellurienylalanine (TePhe), an analog of phenylalanine that contains a tellurium atom, as a small-molecule probe for directly measuring protein synthesis quickly and in a wide range of contexts. Using TePhe to monitor protein synthesis overcomes challenges with existing techniques, as TePhe is an excellent Phe isostere, allowing it to be incorporated into proteins with the native translation machinery without amino acid starvation in vitro and in vivo. TePhe incorporation can be measured by mass cytometry techniques, allowing it to be multiplexed in deep profiling procedures. Furthermore, the unique properties of tellurium suggest promising applications of TePhe in X-ray crystallography, NMR spectroscopy, and imaging of translation in vivo with temporal resolution.

TePhe, a tellurium-containing phenylalanine mimic, allows monitoring of protein synthesis in vivo with mass cytometry